ID   PTPA1_KLULA             Reviewed;         353 AA.
AC   Q6CYH1;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Serine/threonine-protein phosphatase 2A activator 1;
DE            EC=5.2.1.8;
DE   AltName: Full=Peptidyl-prolyl cis-trans isomerase PTPA-1;
DE            Short=PPIase PTPA-1;
DE            Short=Rotamase PTPA-1;
DE   AltName: Full=Phosphotyrosyl phosphatase activator 1;
GN   Name=RRD1; OrderedLocusNames=KLLA0A00462g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases
CC       modulating their activity or substrate specificity, probably by
CC       inducing a conformational change in the catalytic subunit, a direct
CC       target of the PPIase. Can reactivate inactive phosphatase PP2A-
CC       phosphatase methylesterase complexes (PP2Ai) in presence of ATP and
CC       Mg(2+) by dissociating the inactive form from the complex (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC         peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC         COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC         ChEBI:CHEBI:83834; EC=5.2.1.8;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PTPA-type PPIase family. {ECO:0000305}.
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DR   EMBL; CR382121; CAH02606.1; -; Genomic_DNA.
DR   RefSeq; XP_451018.1; XM_451018.1.
DR   AlphaFoldDB; Q6CYH1; -.
DR   SMR; Q6CYH1; -.
DR   STRING; 28985.XP_451018.1; -.
DR   EnsemblFungi; CAH02606; CAH02606; KLLA0_A00462g.
DR   GeneID; 2896400; -.
DR   KEGG; kla:KLLA0_A00462g; -.
DR   eggNOG; KOG2867; Eukaryota.
DR   HOGENOM; CLU_030733_2_1_1; -.
DR   InParanoid; Q6CYH1; -.
DR   OMA; LACRDWH; -.
DR   Proteomes; UP000000598; Chromosome A.
DR   GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000159; C:protein phosphatase type 2A complex; IEA:EnsemblFungi.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019211; F:phosphatase activator activity; IEA:InterPro.
DR   GO; GO:0019888; F:protein phosphatase regulator activity; IEA:EnsemblFungi.
DR   GO; GO:0006914; P:autophagy; IEA:EnsemblFungi.
DR   GO; GO:0006281; P:DNA repair; IEA:EnsemblFungi.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:EnsemblFungi.
DR   GO; GO:0007052; P:mitotic spindle organization; IEA:EnsemblFungi.
DR   GO; GO:0043618; P:regulation of transcription from RNA polymerase II promoter in response to stress; IEA:EnsemblFungi.
DR   GO; GO:0006970; P:response to osmotic stress; IEA:EnsemblFungi.
DR   CDD; cd04087; PTPA; 1.
DR   Gene3D; 1.20.120.1150; -; 1.
DR   InterPro; IPR004327; Phstyr_phstse_ac.
DR   InterPro; IPR043170; PTPA_C_lid.
DR   InterPro; IPR037218; PTPA_sf.
DR   PANTHER; PTHR10012; PTHR10012; 1.
DR   Pfam; PF03095; PTPA; 1.
DR   PIRSF; PIRSF016325; Phstyr_phstse_ac; 1.
DR   SUPFAM; SSF140984; SSF140984; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Isomerase; Nucleus; Reference proteome; Rotamase.
FT   CHAIN           1..353
FT                   /note="Serine/threonine-protein phosphatase 2A activator 1"
FT                   /id="PRO_0000226101"
FT   REGION          331..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..347
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   353 AA;  41004 MW;  89CED35012A86F17 CRC64;
     MDFDYENAKF SMPEKRIFDS QGTLDFQNSV AMVRIQYHLQ KYITLCKGQQ IPDTIKESFF
     TNIVVELLKR LSALIDETPP ERMHSRYGNL SYRDWQTKFQ NQLENWLHEL LPEKYNNSII
     ELSYYISNAF GSKERIDYGT GHELSFLAVI ICLDMLKIET IKGPALLYCF NSYYDVIQKL
     ILTYKLEPAG SHGVWGLDDH FHFSYILGAT QLLDVNTSLI PKDISNTRLM EQNSSSNLFC
     KSIRFINVVK SGPFSNHSPL LYNISRSVHT WHKMQQGLIK MYKVEVLNKF PVVQHFWFGT
     AFFPWTSYGN NHSLPIYQPA ENNDDADFLT ANNATTKMPP PLSTSTSRFI HRR